EMDB-16859: Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosome...

Basic information

Entry

Database: EMDB / ID: EMD-16859

• Title: Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)

Sample

• Complex: BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes
  • Complex: DNA, Histones and Polyubiquitin-B
    • DNA: DNA (142-MER)
    • Protein or peptide: Histone H3.1
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • Protein or peptide: Histone H2A type 1
    • Protein or peptide: Histone H4
    • Protein or peptide: Ubiquitin
  • Complex: BRCA1 associated RING domain 1
    • Protein or peptide: BRCA1 associated RING domain 1

• Keywords: BRCA1-BARD1 / chromatin recognition / nucleosomes / ubiquitin / DNA BINDING PROTEIN

Function / homology

Function:

BRCA1-BARD1 complex / BRCA1-A complex / protein K6-linked ubiquitination / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / negative regulation of megakaryocyte differentiation / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / protein localization to CENP-A containing chromatin / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / Chromatin modifying enzymes / InlA-mediated entry of Listeria monocytogenes into host cells / Regulation of pyruvate metabolism / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Replacement of protamines by nucleosomes in the male pronucleus / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Pexophagy / CENP-A containing nucleosome / VLDLR internalisation and degradation / Regulation of PTEN localization / Packaging Of Telomere Ends / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / TICAM1, RIP1-mediated IKK complex recruitment / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / IKK complex recruitment mediated by RIP1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of activated PAK-2p34 by proteasome mediated degradation / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / TNFR1-induced NF-kappa-B signaling pathway / PINK1-PRKN Mediated Mitophagy / telomere organization / TCF dependent signaling in response to WNT / Interleukin-7 signaling / Inhibition of DNA recombination at telomere / RNA Polymerase I Promoter Opening / Meiotic synapsis / Autodegradation of Cdh1 by Cdh1:APC/C / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / APC/C:Cdc20 mediated degradation of Securin / activated TAK1 mediates p38 MAPK activation / Regulation of NF-kappa B signaling / Assembly of the ORC complex at the origin of replication / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / Regulation of signaling by CBL / NIK-->noncanonical NF-kB signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / SCF-beta-TrCP mediated degradation of Emi1 / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / TNFR2 non-canonical NF-kB pathway / Negative regulation of FGFR3 signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / DNA methylation / Fanconi Anemia Pathway / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex

Domain/homology:

BARD1, Zinc finger, RING-type / zf-RING of BARD1-type protein / BRCA1 C Terminus (BRCT) domain / breast cancer carboxy-terminal domain / BRCT domain profile. / BRCT domain / BRCT domain superfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / : / Histone H2B signature. / Histone H2A conserved site / Histone H2A signature. / Histone H2B / Histone H2B / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone 2A / Histone H2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / : / Ankyrin repeat / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin conserved site / Zinc finger RING-type profile. / Ankyrin repeat-containing domain superfamily / Histone H3 signature 1. / Zinc finger, RING-type / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily

Component:

BRCA1-associated RING domain protein 1 / Histone H2A type 1 / Polyubiquitin-C / Histone H4 / Histone H2B type 1-C/E/F/G/I / Histone H3.1

• Biological species: Homo sapiens (human) / Felis catus (domestic cat)
• Method: single particle reconstruction / cryo EM / Resolution: 3.4 Å
• Authors: Foglizzo M / Burdett H / Wilson MD / Zeqiraj E

Funding support

United Kingdom, 4 items

Organization	Grant number	Country
Medical Research Council (MRC, United Kingdom)	MR/T029471/1	United Kingdom
Wellcome Trust	222531/Z/21/Z	United Kingdom
Wellcome Trust	108466/Z/15/Z	United Kingdom
Wellcome Trust	221524/Z/20/Z	United Kingdom

• Citation: Journal: Nucleic Acids Res / Year: 2023; Title: BRCA1-BARD1 combines multiple chromatin recognition modules to bridge nascent nucleosomes.; Authors: Hayden Burdett / Martina Foglizzo / Laura J Musgrove / Dhananjay Kumar / Gillian Clifford / Lisa J Campbell / George R Heath / Elton Zeqiraj / Marcus D Wilson / ; Abstract: Chromatin association of the BRCA1-BARD1 heterodimer is critical to promote homologous recombination repair of DNA double-strand breaks (DSBs) in S/G2. How the BRCA1-BARD1 complex interacts with chromatin that contains both damage induced histone H2A ubiquitin and inhibitory H4K20 methylation is not fully understood. We characterised BRCA1-BARD1 binding and enzymatic activity to an array of mono- and di-nucleosome substrates using biochemical, structural and single molecule imaging approaches. We found that the BRCA1-BARD1 complex preferentially interacts and modifies di-nucleosomes over mono-nucleosomes, allowing integration of H2A Lys-15 ubiquitylation signals with other chromatin modifications and features. Using high speed- atomic force microscopy (HS-AFM) to monitor how the BRCA1-BARD1 complex recognises chromatin in real time, we saw a highly dynamic complex that bridges two nucleosomes and associates with the DNA linker region. Bridging is aided by multivalent cross-nucleosome interactions that enhance BRCA1-BARD1 E3 ubiquitin ligase catalytic activity. Multivalent interactions across nucleosomes explain how BRCA1-BARD1 can recognise chromatin that retains partial di-methylation at H4 Lys-20 (H4K20me2), a parental histone mark that blocks BRCA1-BARD1 interaction with nucleosomes, to promote its enzymatic and DNA repair activities.

History

Deposition	Mar 15, 2023	-
Header (metadata) release	Oct 11, 2023	-
Map release	Oct 11, 2023	-
Update	Nov 22, 2023	-
Current status	Nov 22, 2023	Processing site: PDBe / Status: Released

Map

• File: Download / File: emd_16859.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
• Voxel size: X=Y=Z: 0.86 Å

Density

Contour Level	By AUTHOR: 0.435
Minimum - Maximum	-2.1360242 - 3.2577093
Average (Standard dev.)	0.008429022 (±0.081438005)

• Symmetry: Space group: 1

Details

EMDB XML:

Map geometry	Axis order X Y Z Origin 0 0 0 Dimensions 320 320 320 Spacing 320 320 320
Cell	A=B=C: 275.2 Å α=β=γ: 90.0 °

Supplemental data

Mask #1

• File: emd_16859_msk_1.map

Additional map: #1

• File: emd_16859_additional_1.map

Additional map: #2

• File: emd_16859_additional_2.map

Half map: #2

• File: emd_16859_half_map_1.map

Half map: #1

• File: emd_16859_half_map_2.map

Sample components

Entire : BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes

• Entire: Name: BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes

Components

• Complex: BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes
  • Complex: DNA, Histones and Polyubiquitin-B
    • DNA: DNA (142-MER)
    • Protein or peptide: Histone H3.1
    • Protein or peptide: Histone H2B type 1-C/E/F/G/I
    • Protein or peptide: Histone H2A type 1
    • Protein or peptide: Histone H4
    • Protein or peptide: Ubiquitin
  • Complex: BRCA1 associated RING domain 1
    • Protein or peptide: BRCA1 associated RING domain 1

Supramolecule #1: BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes

• Supramolecule: Name: BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
• Molecular weight: Theoretical: 246 KDa

Supramolecule #2: DNA, Histones and Polyubiquitin-B

• Supramolecule: Name: DNA, Histones and Polyubiquitin-B / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#5, #7
• Source (natural): Organism: Homo sapiens (human)

Supramolecule #3: BRCA1 associated RING domain 1

• Supramolecule: Name: BRCA1 associated RING domain 1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #6
• Source (natural): Organism: Felis catus (domestic cat)

Macromolecule #1: DNA (142-MER)

• Macromolecule: Name: DNA (142-MER) / type: dna / ID: 1 / Number of copies: 2 / Classification: DNA
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 108.097586 KDa

Sequence

String:

(DA)(DA)(DT)(DA)(DC)(DG)(DC)(DG)(DG)(DC) (DC)(DG)(DC)(DC)(DC)(DT)(DG)(DG)(DA)(DG) (DA)(DA)(DT)(DC)(DC)(DC)(DG)(DG)(DT) (DG)(DC)(DC)(DG)(DA)(DG)(DG)(DC)(DC)(DG) (DC) (DT)(DC)(DA)(DA)(DT)(DT)(DG)(DG) (DT)(DC)(DG)(DT)(DA)(DG)(DA)(DC)(DA)(DG) (DC)(DT) (DC)(DT)(DA)(DG)(DC)(DA)(DC) (DC)(DG)(DC)(DT)(DT)(DA)(DA)(DA)(DC)(DG) (DC)(DA)(DC) (DG)(DT)(DA)(DC)(DG)(DC) (DG)(DC)(DT)(DG)(DT)(DC)(DC)(DG)(DC)(DC) (DG)(DC)(DG)(DT) (DT)(DT)(DT)(DA)(DA) (DC)(DC)(DG)(DC)(DC)(DA)(DA)(DG)(DG)(DG) (DG)(DA)(DT)(DT)(DA) (DC)(DT)(DC)(DC) (DC)(DT)(DA)(DG)(DT)(DC)(DT)(DC)(DC)(DA) (DG)(DG)(DC)(DA)(DC)(DG) (DT)(DG)(DT) (DC)(DA)(DG)(DA)(DT)(DA)(DT)(DA)(DT)(DA) (DC)(DA)(DT)(DC)(DC)(DT)(DG) (DT)(DG) (DC)(DA)(DA)(DT)(DG)(DT)(DG)(DT)(DT)(DC) (DC)(DA)(DT)(DA)(DT)(DG)(DG)(DA) (DA) (DC)(DA)(DC)(DA)(DT)(DT)(DG)(DC)(DA)(DC) (DA)(DG)(DG)(DA)(DT)(DG)(DT)(DA)(DT) (DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA)(DC)(DA) (DC)(DG)(DT)(DG)(DC)(DC)(DT)(DG)(DG)(DA) (DG)(DA)(DC)(DT)(DA)(DG)(DG)(DG)(DA) (DG)(DT)(DA)(DA)(DT)(DC)(DC)(DC)(DC)(DT) (DT) (DG)(DG)(DC)(DG)(DG)(DT)(DT)(DA) (DA)(DA)(DA)(DC)(DG)(DC)(DG)(DG)(DC)(DG) (DG)(DA) (DC)(DA)(DG)(DC)(DG)(DC)(DG) (DT)(DA)(DC)(DG)(DT)(DG)(DC)(DG)(DT)(DT) (DT)(DA)(DA) (DG)(DC)(DG)(DG)(DT)(DG) (DC)(DT)(DA)(DG)(DA)(DG)(DC)(DT)(DG)(DT) (DC)(DT)(DA)(DC) (DG)(DA)(DC)(DC)(DA) (DA)(DT)(DT)(DG)(DA)(DG)(DC)(DG)(DG)(DC) (DC)(DT)(DC)(DG)(DG) (DC)(DA)(DC)(DC) (DG)(DG)(DG)(DA)(DT)(DT)(DC)(DT)(DC)(DC) (DA)(DG)(DG)(DG)(DC)(DG) (DG)(DC)(DC) (DG)(DC)(DG)(DT)(DA)(DT)(DT)

Macromolecule #2: Histone H3.1

• Macromolecule: Name: Histone H3.1 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 15.366088 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEACEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGER

UniProtKB: Histone H3.1

Macromolecule #3: Histone H2B type 1-C/E/F/G/I

• Macromolecule: Name: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 13.937213 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK

UniProtKB: Histone H2B type 1-C/E/F/G/I

Macromolecule #4: Histone H2A type 1

• Macromolecule: Name: Histone H2A type 1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 14.121537 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG KVTIAQGGVL PNIQAVLLPK KTESHHKAKG K

UniProtKB: Histone H2A type 1

Macromolecule #5: Histone H4

• Macromolecule: Name: Histone H4 / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 11.394426 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

UniProtKB: Histone H4

Macromolecule #6: BRCA1 associated RING domain 1

• Macromolecule: Name: BRCA1 associated RING domain 1 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
• Source (natural): Organism: Felis catus (domestic cat)
• Molecular weight: Theoretical: 85.897531 KDa
• Recombinant expression: Organism: Trichoplusia ni (cabbage looper)

Sequence

String:

MPGNRQLRVR SGNEPRPAPA MEPEGRGAWA HSRAAFDRLE KLLRCSRCTN ILREPVCLGG CEHIFCSNCV SDCIGTGCPV CYTPAWIQD VKINRQLDSM IQLCSKLRNL LHDNKLSDLK EDTSRQNVFN DAENKKNSIK MWFSPRSKKV RYVVTKVSVQ T QPQVIDDG NAQQASVYKF VSTSPPTSVP ERAKKASTRS RKKQKKKTLA EINQEWNFEA EKEDGEPDSK EEFKEKLVSF CS QPSVIAS PQTNGGIDLL ASDSVTESEC SRSLTEVSLP LAEQIESPET GSRNEDATPE KNACVDHLTS KQPLPSGHNG RPG RRSRRS SPVSKRCRSS IPGTSGQQML LSENKPLPGC SSPPPSKRKV GDTLRRKNSN ISDESMSLSP GTPPSTLNSP SYRR MMFSP SAVKLSPGSL TAVKRNHRGE TLLHIASIKG DLPSVEYLLQ NGSDPNVKDH AGWTPLHEAC NHGHLKVVEL LLQHK ALVN STGYQNDSPL HDAAKNGHMD IVKLLLSYGA SRNAVNIFGL RPVDYADGEN MKSLLLLPEQ NESSSTRHCS VTNTGQ RRD GPLVLIGSGL SSEQQKMLSE LAVILKAKKC AEFDSTVTHV IVPGDTVQST LKCMLGILNG CWILKFEWVK ACLQRKA CE QEEKYEIPEG PQRSRLNKEQ LLPKLFDGCY FYFGGAFKHH PKDNLVKLVT AAGGQVLSRK PKPDSDVTQT INTVAYHA K ADSDQRFCTQ YIIYEDLSNH RPERVRQGKV WMAPSSWFID CVMSFELLPL DS

UniProtKB: BRCA1-associated RING domain protein 1

Macromolecule #7: Ubiquitin

• Macromolecule: Name: Ubiquitin / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
• Source (natural): Organism: Homo sapiens (human)
• Molecular weight: Theoretical: 8.576831 KDa
• Recombinant expression: Organism: Escherichia coli (E. coli)

Sequence

String:

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG

UniProtKB: Polyubiquitin-C

Experimental details

Structure determination

• Method: cryo EM
• Processing: single particle reconstruction
• Aggregation state: particle

Sample preparation

• Concentration: 1 mg/mL

Buffer

pH: 7.5
Component:

Concentration	Formula	Name
20.0 mM	HEPES	4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
50.0 mM	NaCl	sodium chloride

Details: 20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT

• Grid: Model: Quantifoil R3.5/1 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR; Details: Quantifoil R3.5/1 200-mesh grids (Quantifoil Micro Tools GmbH) were glow-discharged for 30 s at 40 mA using a GloQube (Quorum) glow discharge unit
• Vitrification: Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV / Details: blot force = 0 N blot time = 8 s.
• Details: Purified cat BRCA1dExon11-FL BARD1 (at 3 uM) was incubated with H2AKc15ub mono-nucleosomes (at 1.5 uM) for 1 h on ice before cryo-EM grids preparation

Electron microscopy

• Microscope: FEI TITAN KRIOS
• Image recording: Film or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 16015 / Average exposure time: 5.0 sec. / Average electron dose: 36.37 e/Ų
• Electron beam: Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
• Electron optics: C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.1 µm / Nominal defocus min: 1.7 µm / Nominal magnification: 96000
• Sample stage: Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
• Experimental equipment: Model: Titan Krios / Image courtesy: FEI Company

Image processing

• Particle selection: Number selected: 7204662
• Startup model: Type of model: OTHER; Details: The start up model was generated directly from this dataset, following 2D Classification and Ab Initio Reconstruction in cryoSPARC 3.2.0
• Final reconstruction: Number classes used: 3 / Applied symmetry - Point group: C₁ (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.0.1) / Number images used: 359954
• Initial angle assignment: Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.2.0)
• Final angle assignment: Type: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.0.1)
• Final 3D classification: Number classes: 6 / Software - Name: cryoSPARC (ver. 4.0.1)

Atomic model buiding 1

• Refinement: Space: REAL

Output model

PDB-8off:
Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)